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Ras-related protein Rab-35 (GTP-binding protein RAY) (Ras-related protein Rab-1C)

 RAB35_HUMAN             Reviewed;         201 AA.
Q15286; B2R6E0; B4E390;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 171.
RecName: Full=Ras-related protein Rab-35;
AltName: Full=GTP-binding protein RAY;
AltName: Full=Ras-related protein Rab-1C;
Name=RAB35; Synonyms=RAB1C, RAY;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=7811277; DOI=10.1006/bbrc.1994.2889;
Zhu A.X., Zhao Y., Flier J.S.;
"Molecular cloning of two small GTP-binding proteins from human
skeletal muscle.";
Biochem. Biophys. Res. Commun. 205:1875-1882(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Tongue, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-22 AND GLN-67.
PubMed=16950109; DOI=10.1016/j.cub.2006.07.020;
Kouranti I., Sachse M., Arouche N., Goud B., Echard A.;
"Rab35 regulates an endocytic recycling pathway essential for the
terminal steps of cytokinesis.";
Curr. Biol. 16:1719-1725(2006).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[11]
ENZYME REGULATION, AND INTERACTION WITH DENND1A; DENND1B AND DENND1C.
PubMed=20154091; DOI=10.1074/jbc.M109.050930;
Marat A.L., McPherson P.S.;
"The connecdenn family, Rab35 guanine nucleotide exchange factors
interfacing with the clathrin machinery.";
J. Biol. Chem. 285:10627-10637(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH L.PNEUMOPHILA ANKX AND DRRA, AMPYLATION AT TYR-77,
AND PHOSPHORYLATION AT SER-75.
PubMed=21822290; DOI=10.1038/nature10335;
Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
"Modulation of Rab GTPase function by a protein phosphocholine
transferase.";
Nature 477:103-106(2011).
[14]
INTERACTION WITH L.PNEUMOPHILA ANKX AND DRRA, AMPYLATION, AND
PHOSPHORYLATION AT SER-75.
PubMed=22307087; DOI=10.1038/emboj.2012.16;
Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A.,
Goody R.S.;
"Reversible phosphocholination of Rab proteins by Legionella
pneumophila effector proteins.";
EMBO J. 31:1774-1784(2012).
[15]
FUNCTION IN ENDOCYTOSIS, SUBCELLULAR LOCATION, AND INTERACTION WITH
MICALL1.
PubMed=21951725; DOI=10.1111/j.1600-0854.2011.01294.x;
Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.;
"MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and
Arf6 with Rab8a.";
Traffic 13:82-93(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-180 IN COMPLEX WITH
DENND1B.
PubMed=22065758; DOI=10.1073/pnas.1110415108;
Wu X., Bradley M.J., Cai Y., Kummel D., De La Cruz E.M., Barr F.A.,
Reinisch K.M.;
"Insights regarding guanine nucleotide exchange from the structure of
a DENN-domain protein complexed with its Rab GTPase substrate.";
Proc. Natl. Acad. Sci. U.S.A. 108:18672-18677(2011).
-!- FUNCTION: The small GTPases Rab are key regulators of
intracellular membrane trafficking, from the formation of
transport vesicles to their fusion with membranes. Rabs cycle
between an inactive GDP-bound form and an active GTP-bound form
that is able to recruit to membranes different sets of downstream
effectors directly responsible for vesicle formation, movement,
tethering and fusion. That Rab is involved in the process of
endocytosis and is an essential rate-limiting regulator of the
fast recycling pathway back to the plasma membrane. During
cytokinesis, required for the postfurrowing terminal steps, namely
for intercellular bridge stability and abscission, possibly by
controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and
SEPT2 localization at the intercellular bridge. May indirectly
regulate neurite outgrowth. Together with TBC1D13 may be involved
in regulation of insulin-induced glucose transporter SLC2A4/GLUT4
translocation to the plasma membrane in adipocytes.
{ECO:0000250|UniProtKB:Q6PHN9, ECO:0000269|PubMed:16950109,
ECO:0000269|PubMed:21951725}.
-!- ENZYME REGULATION: Rab activation is generally mediated by a
guanine exchange factor (GEF), while inactivation through
hydrolysis of bound GTP is catalyzed by a GTPase activating
protein (GAP) (PubMed:20154091). That Rab is activated by the
guanine exchange factors DENND1A, DENND1B and DENND1C
(PubMed:20154091). {ECO:0000269|PubMed:20154091}.
-!- SUBUNIT: Interacts with DENND1A and DENND1B; in a nucleotide-
dependent manner (PubMed:20154091, PubMed:22065758). Interacts
with DENND1C; weak interaction which is nucleotide-independent
(PubMed:20154091). Interacts (GTP-bound form) with ACAP2 and
MICALL1; the interaction is direct and probably recruits ACAP2 and
MICALL1 to membranes (PubMed:21951725). Interacts with EHD1; the
interaction is indirect through MICALL1 and probably recruits EHD1
to membranes (By similarity). {ECO:0000250|UniProtKB:Q6PHN9,
ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:21951725,
ECO:0000269|PubMed:22065758}.
-!- INTERACTION:
Q8N3F8:MICALL1; NbExp=2; IntAct=EBI-722275, EBI-1056885;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16950109,
ECO:0000269|PubMed:21951725}; Lipid-anchor {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Membrane, clathrin-coated pit
{ECO:0000269|PubMed:16950109}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000269|PubMed:16950109}. Endosome
{ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725}.
Melanosome {ECO:0000269|PubMed:17081065}. Note=Present on sorting
endosomes and recycling endosome tubules (PubMed:16950109). Tends
to be enriched in PIP2-positive cell membrane domains
(PubMed:16950109). During mitosis, associated with the plasma
membrane and present at the ingressing furrow during early
cytokinesis as well as at the intercellular bridge later during
cytokinesis (PubMed:16950109). Identified in stage I to stage IV
melanosomes (PubMed:17081065). {ECO:0000269|PubMed:16950109,
ECO:0000269|PubMed:17081065}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15286-1; Sequence=Displayed;
Name=2;
IsoId=Q15286-2; Sequence=VSP_042918;
Note=No experimental confirmation available.;
-!- PTM: AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the
switch 2 region and leads to moderate inactivation of the GTPase
activity. It appears to prolong the lifetime of the GTP state of
RAB1B by restricting access of GTPase effectors to switch 2 and
blocking effector-stimulated GTP hydrolysis, thereby rendering
RAB35 constitutively active. {ECO:0000269|PubMed:21822290,
ECO:0000269|PubMed:22307087}.
-!- PTM: Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and
GTP-bound forms can be phosphocholinated. Phosphocholination
inhibits the GEF activity of DENND1A.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; X79781; CAA56177.1; -; mRNA.
EMBL; AF498960; AAM21108.1; -; mRNA.
EMBL; BT020024; AAV38827.1; -; mRNA.
EMBL; CR536486; CAG38725.1; -; mRNA.
EMBL; CR541683; CAG46484.1; -; mRNA.
EMBL; AK304620; BAG65402.1; -; mRNA.
EMBL; AK312538; BAG35437.1; -; mRNA.
EMBL; AC004812; AAC83182.1; -; Genomic_DNA.
EMBL; CH471054; EAW98163.1; -; Genomic_DNA.
EMBL; CH471054; EAW98164.1; -; Genomic_DNA.
EMBL; BC015931; AAH15931.1; -; mRNA.
CCDS; CCDS41846.1; -. [Q15286-1]
CCDS; CCDS53836.1; -. [Q15286-2]
PIR; JC2488; JC2488.
RefSeq; NP_001161078.1; NM_001167606.1. [Q15286-2]
RefSeq; NP_006852.1; NM_006861.6. [Q15286-1]
UniGene; Hs.524788; -.
PDB; 3TW8; X-ray; 2.10 A; B/D=1-180.
PDBsum; 3TW8; -.
ProteinModelPortal; Q15286; -.
SMR; Q15286; -.
BioGrid; 116211; 33.
IntAct; Q15286; 27.
MINT; MINT-1370578; -.
STRING; 9606.ENSP00000229340; -.
iPTMnet; Q15286; -.
PhosphoSitePlus; Q15286; -.
SwissPalm; Q15286; -.
BioMuta; RAB35; -.
DMDM; 3024525; -.
EPD; Q15286; -.
MaxQB; Q15286; -.
PaxDb; Q15286; -.
PeptideAtlas; Q15286; -.
PRIDE; Q15286; -.
TopDownProteomics; Q15286-1; -. [Q15286-1]
TopDownProteomics; Q15286-2; -. [Q15286-2]
DNASU; 11021; -.
Ensembl; ENST00000229340; ENSP00000229340; ENSG00000111737. [Q15286-1]
Ensembl; ENST00000534951; ENSP00000441883; ENSG00000111737. [Q15286-2]
GeneID; 11021; -.
KEGG; hsa:11021; -.
UCSC; uc001txm.2; human. [Q15286-1]
CTD; 11021; -.
DisGeNET; 11021; -.
EuPathDB; HostDB:ENSG00000111737.11; -.
GeneCards; RAB35; -.
HGNC; HGNC:9774; RAB35.
HPA; HPA054146; -.
MIM; 604199; gene.
neXtProt; NX_Q15286; -.
OpenTargets; ENSG00000111737; -.
PharmGKB; PA34127; -.
eggNOG; KOG0079; Eukaryota.
eggNOG; ENOG4111IWZ; LUCA.
GeneTree; ENSGT00900000140786; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; Q15286; -.
KO; K07876; -.
OMA; EEMFMAI; -.
OrthoDB; EOG091G0LA6; -.
PhylomeDB; Q15286; -.
TreeFam; TF105954; -.
Reactome; R-HSA-8854214; TBC/RABGAPs.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; RAB35; human.
GeneWiki; RAB35; -.
GenomeRNAi; 11021; -.
PRO; PR:Q15286; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111737; -.
CleanEx; HS_RAB35; -.
ExpressionAtlas; Q15286; baseline and differential.
Genevisible; Q15286; HS.
GO; GO:0031253; C:cell projection membrane; IDA:UniProtKB.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0048227; P:plasma membrane to endosome transport; IMP:UniProtKB.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Coated pit;
Complete proteome; Cytoplasmic vesicle; Endosome; GTP-binding;
Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
Prenylation; Protein transport; Reference proteome; Transport.
CHAIN 1 201 Ras-related protein Rab-35.
/FTId=PRO_0000121245.
NP_BIND 15 22 GTP. {ECO:0000250}.
NP_BIND 63 67 GTP. {ECO:0000250}.
NP_BIND 120 123 GTP. {ECO:0000250}.
MOTIF 37 45 Effector region. {ECO:0000250}.
MOD_RES 72 72 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 75 75 O-(2-cholinephosphoryl)serine.
{ECO:0000305|PubMed:21822290,
ECO:0000305|PubMed:22307087}.
MOD_RES 77 77 O-AMP-tyrosine.
{ECO:0000305|PubMed:21822290}.
LIPID 200 200 S-geranylgeranyl cysteine. {ECO:0000250}.
LIPID 201 201 S-geranylgeranyl cysteine. {ECO:0000250}.
VAR_SEQ 118 201 VGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVE
EMFNCITELVLRAKKDNLAKQQQQQQNDVVKLTKNSKRKKR
CC -> DVQLHHGAGPPSKERQPGKTAAATTERCGEAHEEQ
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042918.
MUTAGEN 22 22 S->N: Destabilization of the
intercellular bridge during cytokinesis.
Strong reduction in fast recycling.
{ECO:0000269|PubMed:16950109}.
MUTAGEN 67 67 Q->L: Loss of GTPase activity. Increased
fast recycling.
{ECO:0000269|PubMed:16950109}.
STRAND 7 14 {ECO:0000244|PDB:3TW8}.
HELIX 21 28 {ECO:0000244|PDB:3TW8}.
TURN 38 40 {ECO:0000244|PDB:3TW8}.
STRAND 41 52 {ECO:0000244|PDB:3TW8}.
STRAND 55 64 {ECO:0000244|PDB:3TW8}.
HELIX 67 69 {ECO:0000244|PDB:3TW8}.
HELIX 75 78 {ECO:0000244|PDB:3TW8}.
STRAND 82 89 {ECO:0000244|PDB:3TW8}.
HELIX 93 109 {ECO:0000244|PDB:3TW8}.
STRAND 113 120 {ECO:0000244|PDB:3TW8}.
HELIX 125 127 {ECO:0000244|PDB:3TW8}.
HELIX 132 142 {ECO:0000244|PDB:3TW8}.
STRAND 146 148 {ECO:0000244|PDB:3TW8}.
TURN 151 154 {ECO:0000244|PDB:3TW8}.
HELIX 157 175 {ECO:0000244|PDB:3TW8}.
SEQUENCE 201 AA; 23025 MW; 31EB15D6D42E076E CRC64;
MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV EINGEKVKLQ
IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK RWLHEINQNC DDVCRILVGN
KNDDPERKVV ETEDAYKFAG QMGIQLFETS AKENVNVEEM FNCITELVLR AKKDNLAKQQ
QQQQNDVVKL TKNSKRKKRC C


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